Among the 17 mycoviruses which have been physically characterized, there are two which code for specific toxins lethal to the non-infected strains of the same fungi. These are the mycoviruses Saccharomyces cerevisiae and Ustilago maydis. These viruses have many similar properties, including segmented dsRNA genomes which may be grouped into classes of heavy (4-6 kbp), medium (0.7-1.4 kbp) and light (less than 0.35 kbp) segments. In both viruses the heavy segments code for capsid production and the medium segments code for toxins. There are three strains of the Ustilago virus which are distinguishable by the number of genomic segments of each class and slight differences in specificity of the toxins. In this project relationships of the dsRNA segments within and among the three strains will be determined using heterodupliex and hybridization procedures. The ability of each segment to be transcribed to mRNA and the translation product of representative dsRNA segments will be determined. Specific dsRNA segments will be cloned in E. coli for the study of amplified gene products and sequence analysis. These studies will provide a better understanding of how toxins coded by viruses interrupt or relate to host cell metabolism. Such basic knowledge will be used in the control of pathogenic fungi or the control of specific toxins secreted by fungi which result in food poisoning.

Agency
National Institute of Health (NIH)
Institute
National Institute of Environmental Health Sciences (NIEHS)
Type
Research Project (R01)
Project #
9R01ES003817-04
Application #
3251538
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1985-05-01
Project End
1989-04-30
Budget Start
1985-05-01
Budget End
1986-04-30
Support Year
4
Fiscal Year
1985
Total Cost
Indirect Cost
Name
University of Utah
Department
Type
Schools of Medicine
DUNS #
City
Salt Lake City
State
UT
Country
United States
Zip Code
84112
Cui, Tie-Zhong; Conte, Annalea; Fox, Jennifer L et al. (2014) Modulation of the respiratory supercomplexes in yeast: enhanced formation of cytochrome oxidase increases the stability and abundance of respiratory supercomplexes. J Biol Chem 289:6133-41
Na, Un; Yu, Wendou; Cox, James et al. (2014) The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur subunit of succinate dehydrogenase. Cell Metab 20:253-66
Bohovych, Iryna; Donaldson, Garrett; Christianson, Sara et al. (2014) Stress-triggered activation of the metalloprotease Oma1 involves its C-terminal region and is important for mitochondrial stress protection in yeast. J Biol Chem 289:13259-72
Patil, Vinay A; Fox, Jennifer L; Gohil, Vishal M et al. (2013) Loss of cardiolipin leads to perturbation of mitochondrial and cellular iron homeostasis. J Biol Chem 288:1696-705
Kim, Hyung J; Winge, Dennis R (2013) Emerging concepts in the flavinylation of succinate dehydrogenase. Biochim Biophys Acta 1827:627-36
Kim, Hyung J; Khalimonchuk, Oleh; Smith, Pamela M et al. (2012) Structure, function, and assembly of heme centers in mitochondrial respiratory complexes. Biochim Biophys Acta 1823:1604-16
Khalimonchuk, Oleh; Kim, Hyung; Watts, Talina et al. (2012) Oligomerization of heme o synthase in cytochrome oxidase biogenesis is mediated by cytochrome oxidase assembly factor Coa2. J Biol Chem 287:26715-26
Khalimonchuk, Oleh; Jeong, Mi-Young; Watts, Talina et al. (2012) Selective Oma1 protease-mediated proteolysis of Cox1 subunit of cytochrome oxidase in assembly mutants. J Biol Chem 287:7289-300
Eletsky, Alexander; Jeong, Mi-Young; Kim, Hyung et al. (2012) Solution NMR structure of yeast succinate dehydrogenase flavinylation factor Sdh5 reveals a putative Sdh1 binding site. Biochemistry 51:8475-7
Kim, Hyung J; Jeong, Mi-Young; Na, Un et al. (2012) Flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunit. J Biol Chem 287:40670-9

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